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Yorodumi- EMDB-51870: Escherichia phage Paracelsus (Bas36) baseplate, proximal tail fib... -
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Open data
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Basic information
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| Title | Escherichia phage Paracelsus (Bas36) baseplate, proximal tail fiber and tail. | ||||||||||||||||||
Map data | Bas36 baseplate, tail, and proximal LTF C6 map | ||||||||||||||||||
Sample |
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Keywords | Baseplate / Tail fiber / Tail tube / Tail sheath / VIRUS | ||||||||||||||||||
| Biological species | Escherichia phage EmilHeitz (virus) | ||||||||||||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 9.5 Å | ||||||||||||||||||
Authors | Klein-Sousa V / Roa-Eguiara A / Taylor NMI | ||||||||||||||||||
| Funding support | Denmark, 5 items
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Citation | Journal: Sci Adv / Year: 2025Title: RBPseg: Toward a complete phage tail fiber structure atlas. Authors: Victor Klein-Sousa / Aritz Roa-Eguiara / Claudia S Kielkopf / Nicholas Sofos / Nicholas M I Taylor / ![]() Abstract: Bacteriophages use receptor-binding proteins (RBPs) to adhere to bacterial hosts, yet their sequence and structural diversity remain poorly understood. Tail fibers, a major class of RBPs, are ...Bacteriophages use receptor-binding proteins (RBPs) to adhere to bacterial hosts, yet their sequence and structural diversity remain poorly understood. Tail fibers, a major class of RBPs, are elongated and flexible trimeric proteins, making their full-length structures difficult to resolve experimentally. Advances in deep learning-based protein structure prediction, such as AlphaFold2-multimer (AF2M) and ESMFold, provide opportunities for studying these challenging proteins. Here, we introduce RBPseg, a method that combines monomeric ESMFold predictions with a structural-based domain identification approach, to divide tail fiber sequences into manageable fractions for high-confidence modeling with AF2M. Using this approach, we generated complete tail fiber models, validated by single-particle cryo-electron microscopy of five fibers from three phages. A structural classification of 67 fibers identified 16 distinct classes and 89 domains, revealing patterns of modularity, convergence, divergence, and domain swapping. Our findings suggest that these structural classes represent at least 24% of the known tail fiber universe, providing key insights into their evolution and functionality. | ||||||||||||||||||
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_51870.map.gz | 17.2 MB | EMDB map data format | |
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| Header (meta data) | emd-51870-v30.xml emd-51870.xml | 16.5 KB 16.5 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_51870_fsc.xml | 9.5 KB | Display | FSC data file |
| Images | emd_51870.png | 52.7 KB | ||
| Masks | emd_51870_msk_1.map | 34.3 MB | Mask map | |
| Filedesc metadata | emd-51870.cif.gz | 4.2 KB | ||
| Others | emd_51870_additional_1.map.gz emd_51870_half_map_1.map.gz emd_51870_half_map_2.map.gz | 15.7 MB 31.7 MB 31.7 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-51870 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-51870 | HTTPS FTP |
-Related structure data
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_51870.map.gz / Format: CCP4 / Size: 34.3 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | Bas36 baseplate, tail, and proximal LTF C6 map | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 4.61538 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Mask #1
| File | emd_51870_msk_1.map | ||||||||||||
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| Density Histograms |
-Additional map: C1 Local refinement map of proximal LTF
| File | emd_51870_additional_1.map | ||||||||||||
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| Annotation | C1 Local refinement map of proximal LTF | ||||||||||||
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| Density Histograms |
-Half map: Half A map
| File | emd_51870_half_map_1.map | ||||||||||||
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| Annotation | Half A map | ||||||||||||
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| Density Histograms |
-Half map: Half B map
| File | emd_51870_half_map_2.map | ||||||||||||
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| Annotation | Half B map | ||||||||||||
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Sample components
-Entire : Escherichia phage EmilHeitz
| Entire | Name: Escherichia phage EmilHeitz (virus) |
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| Components |
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-Supramolecule #1: Escherichia phage EmilHeitz
| Supramolecule | Name: Escherichia phage EmilHeitz / type: virus / ID: 1 / Parent: 0 Details: Phage was amplified in liquid media by E. Coli MG1655 dRM infection, and purified using PEG precipitation and Opti-Prep Gradient. NCBI-ID: 2852021 / Sci species name: Escherichia phage EmilHeitz / Virus type: VIRION / Virus isolate: SPECIES / Virus enveloped: No / Virus empty: No |
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| Host (natural) | Organism: ![]() |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 7.5 Component:
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| Grid | Model: UltrAuFoil R2/2 / Support film - Material: CARBON / Support film - topology: CONTINUOUS / Support film - Film thickness: 0.2 | ||||||||||||
| Vitrification | Cryogen name: ETHANE / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
| Microscope | TFS KRIOS |
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| Image recording | Film or detector model: TFS FALCON 4i (4k x 4k) / Average electron dose: 40.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 0.5 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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About Yorodumi



Escherichia phage EmilHeitz (virus)
Keywords
Authors
Denmark, 5 items
Citation

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Processing
FIELD EMISSION GUN

